PMID:6363404
| Citation |
Amanuma, H and Strominger, JL (1984) Purification and properties of penicillin-binding proteins 5 and 6 from the dacA mutant strain of Escherichia coli (JE 11191). J. Biol. Chem. 259:1294-8 |
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| Abstract |
Penicillin-binding proteins 5 and 6 have been purified to homogeneity from the dacA mutant strain of Escherichia coli (JE 11191). Protein 6 from the mutant strain appears to be identical to that from the wild type, but protein 5 is a mutant protein which has no D-alanine carboxypeptidase activity. Moreover, the mutant protein 5 binds, but does not release, [14C]penicillin G. Correspondingly, an acyl-enzyme intermediate derived from a synthetic substrate is accumulated by the mutant protein. A comparison of the acylation site for the synthetic substrate and for penicillin G by limited proteolysis and some other properties of the mutant protein are described. |
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| Keywords |
Acylation; Bacterial Proteins; Carrier Proteins/isolation & purification; Chromatography, Ion Exchange; Electrophoresis, Polyacrylamide Gel; Escherichia coli/analysis; Escherichia coli/genetics; Hexosyltransferases; Hydrogen-Ion Concentration; Muramoylpentapeptide Carboxypeptidase; Mutation; Penicillin G/metabolism; Penicillin-Binding Proteins; Peptidyl Transferases |
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